Name | Number of supported studies | Average coverage | |
---|---|---|---|
hepatocyte | 6 studies | 72% ± 30% | |
endothelial cell of sinusoid | 4 studies | 27% ± 11% | |
cholangiocyte | 4 studies | 72% ± 20% | |
hepatic stellate cell | 3 studies | 53% ± 29% |
Name | Number of supported studies | Average coverage | |
---|---|---|---|
liver | 4 studies | 57% ± 25% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
liver | 100% | 178169.13 | 226 / 226 | 100% | 7236.81 | 404 / 406 |
pancreas | 100% | 3611.21 | 328 / 328 | 79% | 70.80 | 141 / 178 |
kidney | 100% | 380.78 | 89 / 89 | 52% | 17.21 | 465 / 901 |
stomach | 82% | 124.58 | 296 / 359 | 37% | 3.48 | 107 / 286 |
breast | 65% | 40.08 | 300 / 459 | 37% | 4.60 | 412 / 1118 |
lung | 74% | 25.30 | 430 / 578 | 27% | 12.12 | 312 / 1155 |
ureter | 0% | 0 | 0 / 0 | 100% | 2.36 | 1 / 1 |
thymus | 94% | 38.92 | 614 / 653 | 3% | 0.20 | 16 / 605 |
intestine | 55% | 19.58 | 529 / 966 | 39% | 14.72 | 203 / 527 |
prostate | 68% | 17.00 | 166 / 245 | 6% | 0.38 | 31 / 502 |
uterus | 55% | 14.85 | 94 / 170 | 19% | 1.87 | 85 / 459 |
ovary | 65% | 14.21 | 117 / 180 | 5% | 1.99 | 22 / 430 |
esophagus | 42% | 12.39 | 613 / 1445 | 22% | 8.24 | 40 / 183 |
peripheral blood | 53% | 225.84 | 494 / 929 | 0% | 0 | 0 / 0 |
spleen | 53% | 261.34 | 128 / 241 | 0% | 0 | 0 / 0 |
skin | 47% | 13.77 | 845 / 1809 | 6% | 0.89 | 27 / 472 |
adrenal gland | 47% | 13.67 | 121 / 258 | 2% | 0.30 | 4 / 230 |
bladder | 29% | 4.90 | 6 / 21 | 19% | 2.35 | 98 / 504 |
brain | 42% | 10.19 | 1101 / 2642 | 1% | 0.07 | 6 / 705 |
blood vessel | 37% | 11.15 | 495 / 1335 | 0% | 0 | 0 / 0 |
adipose | 28% | 30.53 | 338 / 1204 | 0% | 0 | 0 / 0 |
heart | 28% | 12.69 | 241 / 861 | 0% | 0 | 0 / 0 |
muscle | 20% | 4.53 | 157 / 803 | 0% | 0 | 0 / 0 |
lymph node | 0% | 0 | 0 / 0 | 3% | 0.17 | 1 / 29 |
tonsil | 0% | 0 | 0 / 0 | 2% | 0.09 | 1 / 45 |
abdomen | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
bone marrow | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
diaphragm | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 80 |
gingiva | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasal cavity | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasopharynx | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nose | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
placenta | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
spinal column | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
GO_0050777 | Biological process | negative regulation of immune response |
GO_0007155 | Biological process | cell adhesion |
GO_0007565 | Biological process | female pregnancy |
GO_0042167 | Biological process | heme catabolic process |
GO_0046329 | Biological process | negative regulation of JNK cascade |
GO_0005615 | Cellular component | extracellular space |
GO_0005576 | Cellular component | extracellular region |
GO_0005886 | Cellular component | plasma membrane |
GO_0070062 | Cellular component | extracellular exosome |
GO_0062023 | Cellular component | collagen-containing extracellular matrix |
GO_0005743 | Cellular component | mitochondrial inner membrane |
GO_0072562 | Cellular component | blood microparticle |
GO_0009986 | Cellular component | cell surface |
GO_0005783 | Cellular component | endoplasmic reticulum |
GO_0005829 | Cellular component | cytosol |
GO_0031965 | Cellular component | nuclear membrane |
GO_0046904 | Molecular function | calcium oxalate binding |
GO_0042803 | Molecular function | protein homodimerization activity |
GO_0019862 | Molecular function | IgA binding |
GO_0004867 | Molecular function | serine-type endopeptidase inhibitor activity |
GO_0030246 | Molecular function | carbohydrate binding |
GO_0016491 | Molecular function | oxidoreductase activity |
GO_0020037 | Molecular function | heme binding |
GO_0019855 | Molecular function | calcium channel inhibitor activity |
GO_0005515 | Molecular function | protein binding |
Gene name | AMBP |
Protein name | Alpha-1-microglobulin/bikunin precursor Protein AMBP Protein AMBP (Protein HC) [Cleaved into: Alpha-1-microglobulin (EC 1.6.2.-) (Alpha-1 microglycoprotein) (Complex-forming glycoprotein heterogeneous in charge); Inter-alpha-trypsin inhibitor light chain (ITI-LC) (Bikunin) (EDC1) (HI-30) (Uronic-acid-rich protein); Trypstatin] |
Synonyms | ITIL HCP |
Description | FUNCTION: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments . Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis . Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential . Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage . Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures . Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation . Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria . Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor . Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). .; FUNCTION: [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion . Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases . As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions . Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization . .; FUNCTION: [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. . FUNCTION: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. . |
Accessions | ENST00000265132.8 ENST00000466610.6 S4R471 P02760 S4R3Y4 ENST00000603230.1 |